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First published online 29 July 2008
doi: 10.1242/jcs.031922

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Dynamics of component exchange at PML nuclear bodies

Stefanie Weidtkamp-Peters^1,*, Thorsten Lenser^2,*, Dmitri Negorev³, Norman Gerstner¹, Thomas G. Hofmann⁴, Georg Schwanitz¹, Christian Hoischen¹, Gerd Maul³, Peter Dittrich² and Peter Hemmerich^1,

¹ Leibniz-Institute of Age Research, Fritz-Lipman-Institute, Beutenbergstr. 11, 07745 Jena, Germany
² Institute of Computer Science, Friedrich-Schiller-University, 07743 Jena, Germany
³ The Wistar Institute, 3601 Spruce Street, Philadelphia, PA 19104, USA
⁴ German Cancer Research Center, Im Neuenheimer Feld 242, 69120 Heidelberg, Germany

Author for correspondence (e-mail: phemmer{at}fli-leibniz.de)

Accepted 27 May 2008

PML nuclear bodies (NBs) are involved in the regulation of key nuclear pathways but their biochemical function in nuclear metabolism is unknown. In this study PML NB assembly dynamics were assessed by live cell imaging and mathematic modeling of its major component parts. We show that all six nuclear PML isoforms exhibit individual exchange rates at NBs and identify PML V as a scaffold subunit. SP100 exchanges at least five times faster at NBs than PML proteins. Turnover dynamics of PML and SP100 at NBs is modulated by SUMOylation. Exchange is not temperature-dependent but depletion of cellular ATP levels induces protein immobilization at NBs. The PML-RAR oncogene exhibits a strong NB retention effect on wild-type PML proteins. HIPK2 requires an active kinase for PML NB targeting and elevated levels of PML IV increase its residence time. DAXX and BLM turn over rapidly and completely at PML NBs within seconds. These findings provide a kinetics model for factor exchange at PML NBs and highlight potential mechanisms to regulate intranuclear trafficking of specific factors at these domains.

Key words: Nuclear body, Promyelocytic leukemia, SP100, SUMO, RAR, Assembly, Kinetics modeling, FRAP, FCS

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